Mecia M. Oliveira
Federal University of Rio de Janeiro
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Environmental Pollution | 2002
Marcelo Einicker-Lamas; Gustavo Antunes Mezian; Thiago Benevides Fernandes; Fabio Leandro S. Silva; Flávio Guerra; Kildare Miranda; Márcia Attias; Mecia M. Oliveira
We have observed the effect of copper and zinc on the biology of Euglena gracilis. The cells displayed different sensitivities to these metals, as the apparent LC50 for Cu2+ was 0.22 mM, and for Zn2+ it was 0.88 mM. While Zn2+ was able to increase cell proliferation even at 0.1 mM, the minimal CuCl2 concentration tested (0.02 mM) was sufficient to impair cell division. Higher concentrations of these metals not only inhibited cell division in a concentration-dependent manner, but also interfered with the metabolism of E. gracilis. A higher accumulation of proteins and lipids per cell was observed at the DI50 concentration for metal-treated cells. These results suggest that the test concentration of both metals leads to a failure in completing cell division. Ultrastructural analysis indicated a chloroplast disorganization in copper-treated cells, as well as the presence of electron dense granules with different shapes and sizes inside vacuoles. Microanalysis of these granules indicated an accumulation of copper, thus suggesting a detoxification role played by the vacuoles. These results indicate that E. gracilis is an efficient biological model for the study of metal poisoning in eukaryotic cells. They also indicate that copper and zinc (copper being more poisonous) had an overall toxic effect on E. gracilis and that part of the effect can be ascribed to defects in the structure of chloroplast membranes.
Zeitschrift für Naturforschung C | 1999
José Roberto Meyer-Fernandes; Mario Alberto da Silva-Neto; Mirna dos Santos Soares; Eloise Fernandes; Anibal E. Vercesi; Mecia M. Oliveira
Abstract Live Trypanosoma cruzi amastigotes hydrolyzed p-nitrophenylphosphate (PNPP), phos-pho-amino-acids and 32P-casein under physiologically appropriate conditions. PNPP was hydrolysed at a rate of 80 nmol ·mg -1 ·h -1 in the presence of 5 mм MgCl2, pH 7.2 at 30 °C. In the absence of Mg2+ the activity was reduced 40% and we call this basal activity. At saturating concentration of PNPP, half-maximal PNPP hydrolysis was obtained with 0.22 mм MgCl2· Ca2+ had no effect on the basal activity, could not substitute Mg2+ as an activator and in contrast inhibited the PNPP hydrolysis stimulated by Mg2+ (I50 = 0.43 mм ) . In the absence of Mg2+ (basal activity) the stimulating half concentration (S0. 5) for PNPP was 1.57 mм , while at saturating MgCl2 concentrations the corresponding S0.5 for PNPP for Mg2+-stimulated phosphatase activity (difference between total minus basal phosphatase activity) was 0.99 mм . The Mg-dependent PNPP hydrolysis was strongly inhibited by sodium fluoride (NaF), vanadate and Zn2+ but not by tartrate and levamizole. The Mg-independent basal phosphatase activity was insensitive to tartrate, levamizole as well NaF and less inhibited by vanadate and Zn2+. Intact amastigotes were also able to hydrolyse phosphoserine, phos-phothreonine and phosphotyrosine but only the phosphotyrosine hydrolysis was stimulated by MgCl2 and inhibited by CaCl2 and phosphotyrosine was a competitive inhibitor of the PNPP hydrolysis stimulated by Mg2+. The cells were also able to hydrolyse 32P-casein phosphorylated on serine and threonine residues but only in the presence of MgCl2. These results indicate that in the amastigote form of T. cruzi there are at least two ectophosphatase activities, one of which is Mg2+ dependent and can dephosphorylate phospho-aminoacids and phosphoproteins under physiological conditions.
Regulatory Peptides | 2005
L.B.A. Rangel; A.G. Lopes; L.S.M. Lara; T.L.G. Carvalho; I.V. Silva; Mecia M. Oliveira; Marcelo Einicker-Lamas; Adalberto Vieyra; L. Nogaroli; Celso Caruso-Neves
In previous papers we showed that Ang II increases the proximal tubule Na+-ATPase activity through AT1/PKC pathway [L.B. Rangel, C. Caruso-Neves, L.S. Lara, A.G. Lopes, Angiotensin II stimulates renal proximal tubule Na+-ATPase activity through the activation of protein kinase C. Biochim. Biophys. Acta 1564 (2002) 310-316, L.B.A. Rangel, A.G. Lopes, L.S. Lara, C. Caruso-Neves, Angiotensin II stimulates renal proximal tubule Na+)-ATPase activity through the activation of protein kinase C. Biochim. Biophys. Acta 1564 (2002) 310-316]. In the present paper, we study the involvement of PI-PLCbeta on the stimulatory effect of angiotensin II (Ang II) on the proximal tubule Na+-ATPase activity. Western blotting assays, using a polyclonal antibody for PI-PLCbeta, show a single band of about 150 KDa, which correspond to PI-PLCbeta isoforms. Ang II induces a rapid decrease in PIP2 levels, a PI-PLCbeta substrate, being the maximal effect observed after 30 s incubation. This effect of Ang II is completely abolished by 5 x 10(-8) M U73122, a specific inhibitor of PI-PLCbeta. In this way, the effect of 10(-8) M Ang II on the proximal tubule basolateral membrane (BLM) Na+-ATPase activity is completely abolished by 5 x 10(-8) M U73122. The increase in diacylglycerol (DAG) concentration, an product of PI-PLCbeta, from 0.1 to 10 nM raises the Na+-ATPase activity from 6.1+/-0.2 to 13.1+/-1.8 nmol Pi mg(-1) min(-1). This effect is similar and non-additive to that observed with Ang II. Furthermore, the stimulatory effect of 10 nM DAG is completely reversed by 10(-8) M calphostin C (Calph C), an inhibitor of PKC. Taken together these data indicate that Ang II stimulates the Na+-ATPase activity of proximal tubule BLM through a PI-PLCbeta/PKC pathway.
Comparative Biochemistry and Physiology B | 1977
Mecia M. Oliveira; S.L. Timm; S.C.G. Costa
1. Lipid composition of Trypanosoma cruzi epimastigote form in culture consist of 35% of phospholipids and 65% of neutral lipids. 2. Among the phospholipids, phosphatidylcholine is the more abundant (44%), followed by phosphatidylethanolamine (28%), phosphatidylinositol (12%), sphingomyelin (4%), and smaller amounts of cardiolipin, phosphatidic acid, lysolecithin, phosphatidylserine (traces), and an unidentified phospholipid (3%). 3. Pulse labeling with 32P showed highest specific incorporation in phosphatidylethanolamine, followed by phosphatidylinositol and phosphatidylcholine, suggesting a more active role for phosphatidylethanolamine in these organisms.
Molecular and Biochemical Parasitology | 1984
Mecia M. Oliveira; Aliete Antunes; Fernando G. de Mello
Intracellular levels of cAMP in Trypanosoma cruzi epimastigotes were determined in the presence of the phosphodiesterase inhibitor 3-isobutyl-1-methylxanthine, and in the presence of the adrenergic ligand isoproterenol. An increase in the levels of cAMP was observed when those drugs were added. This effect was more pronounced when the cells were in the lag phase of growth. Phosphodiesterase inhibitors, catecholamines and dibutyryl cAMP inhibited proliferation of the organisms, as well as [3H]thymidine incorporation in in vitro experiments. These findings strongly suggest that cAMP plays a role in the control of growth of T. cruzi. The effects of adrenergic ligands in increasing cAMP levels and inhibiting growth could be reversed by beta-adrenergic antagonists, suggesting the presence of a receptor-mediated adenylate cyclase system in T. cruzi. Cholinergic ligands had no effect.
Regulatory Peptides | 2005
Iranaia Assunção-Miranda; Adilson L. Guilherme; Clédson Reis-Silva; Glória Costa-Sarmento; Mecia M. Oliveira; Adalberto Vieyra
Angiotensin II (Ang II) increases the cytosolic Ca2+ concentration in different cell types. In this study, we investigate the effect of Ang II on the Ca2+ ATPase of purified basolateral membranes of kidney proximal tubules. This enzyme pumps Ca2+ out of the cytosol in a reaction coupled to ATP hydrolysis, and it is responsible for the fine-tuned regulation of cytosolic Ca2+ activity. Ca2+-ATPase activity is inhibited by picomolar concentrations of Ang II, with maximal inhibition being attained at approximately 50% of the control values. The presence of raising concentrations (10(-11) to 10(-7) M) of losartan (an AT1-receptor antagonist) or PD123319 (an AT2-receptor antagonist) gradually reverts inhibition by Ang II. Both the phospholipase C (PLC) inhibitor U-73122 (10(-6) M) and the inhibitor of protein kinase C (PKC) staurosporine (10(-7) M) prevent inhibition of the Ca2+ pump by Ang II. Incubation of the previously isolated membranes with a PKC activator-the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (10(-8) M)-mimics the inhibition found with Ang II, and the effects of the compounds are not additive. Taken as a whole, these results indicate the Ang II inhibits Ca2+-ATPase by activation of a PKC system present in primed state in these membranes after binding of the hormone to losartan- and PD123319-sensitive receptors coupled to a PLC. Therefore, inhibition of the basolateral membrane Ca2+-ATPase by kinase-mediated phosphorylation appears to be one of the pathways by which Ang II promotes an increase in the cytosolic Ca2+ concentration of proximal tubule cells.
Molecular and Cellular Biochemistry | 1993
Mecia M. Oliveira; Eliane D. Rocha; Edson Rondinelli; Andrea V. Arnholdt; Julio Scharfstein
Fetal calf serum (FCS), which is mitogenic for the pathogenic protozoaT. cruzi, inhibits cAMP production in basal and forskolin-stimulated epimastigotes. It also activates phosphoinositides hydrolysis yielding diacylglycerol and inositol phosphates (Ins-P). Ins-P production is enhanced by AlF4-, GTP or β-γ-methylene-GTP, thus implying G proteins mediation in the phenomenon. An enzyme with phospholipase C activity which may be involved in the phospholipid metabolism was partially characterized.
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology | 1987
Solange L. de Castro; Mecia M. Oliveira
A direct radioligand binding technique utilizing the beta-adrenergic antagonist [3H]dihydroalprenolol was employed in the identification and characterization of Trypanosoma cruzi beta-adrenergic receptors. [3H]DHA binding was saturable (Bmax = 1.5 pmol/10(6) cells) with an apparent equilibrium dissociation constant (Kd) of 127 nM. Binding of [3H]DHA was displaced by propranolol in a concentration-dependent manner. The relative potency order of adrenergic ligands in displacing [3H]DHA binding was: propranolol greater than or equal to alprenolol greater than epinephrine. 5-Hydroxytryptamine, phentolamine and catechol had no effect. The experimental results support the suggestion that beta-adrenergic receptors are present in the pathogenic protozoa Trypanosoma cruzi.
Zeitschrift für Naturforschung C | 1999
Celso Caruso-Neves; Marcelo Einicker-Lamas; Carlos Chagas; Mecia M. Oliveira; Adalberto Vieyra; A.G. Lopes
In the present paper, the presence of a ouabain-insensitive Na+-stimulated, Mg2+-dependent ATPase activity in T. cruzi epimastigotes CL14 clone and Y strain was investigated. The increase in Na+ concentration (from 5 to 170 mᴍ), in the presence of 2 mᴍ ouabain, increases the ATPase activity in a saturable manner along a rectangular hyperbola. The was 18.0 ± 1.0 and 21.1 ± 1.1 nmoles Pi x mg-1 x min-1 and the half-activation value (K50) for Na+ was 34.3 ± 5.8 mᴍ and 37.7 ± 5.3 in CL14 clone and in Y strain, respectively. The Na+-stimulated ATPase activity was inhibited by 5-[aminosulfonyl]-4-chloro-2-[(2-furanylmethyl)-amino] benzoic acid (furosemide) in a dose-dependent manner. The half-inhibition value (I50) was 0.22 ± 0.03 and 0.24 ± 0.07 mᴍ, and the Hill number (n) was 0.99 ± 0.2 and 2.16 ± 0.29 for CL14 clone and Y strain, respectively. These data indicate that both cell types express the ouabain-insensitive Na+-ATPase activity, which might be considered the biochemical expression of the second Na+ pump
Zeitschrift für Naturforschung C | 1998
Celso Caruso-Neves; Marcelo Einicker-Lamas; Carlos Chagas; Mecia M. Oliveira; Adalberto Vieyra; A.G. Lopes
Abstract The presence of (Na++K+)ATPase activity in CL14 clone and NIH NTY strain of Trypanosoma cruzi epimastigotes is demonstrated. A Na+ plus K+ stimulated ATPase activity is found in both strains. The optimal Na+/K+ ratio is 5:1 and 9:1 in CL14 clone and NIH NTY strain, respectively. In both strains, vanadate completely inhibits the ouabain-sensitive ATPase activity indicating that it belongs to the P-type (E 1/E2) family of ion-transporting ATPases. The I50 for vanadate is 0.66 ± 0.04 and 0.04 ± 0.02 μᴍ in CL14 clone and NIH NTY strain, respectively. These data indicate that both strains of T. cruzi epimastigotes express the oua bain-and vanadate-sensitive (Na++K+)ATPase activity. On the other hand, the discrepancy between the parameters analyzed for the inhibitors suggests that they express different iso forms of this enzyme.